pubmed-article:7507482 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7507482 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
pubmed-article:7507482 | lifeskim:mentions | umls-concept:C0025519 | lld:lifeskim |
pubmed-article:7507482 | lifeskim:mentions | umls-concept:C0907533 | lld:lifeskim |
pubmed-article:7507482 | lifeskim:mentions | umls-concept:C0022702 | lld:lifeskim |
pubmed-article:7507482 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:7507482 | lifeskim:mentions | umls-concept:C0243077 | lld:lifeskim |
pubmed-article:7507482 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:7507482 | pubmed:dateCreated | 1994-2-25 | lld:pubmed |
pubmed-article:7507482 | pubmed:abstractText | Nitric oxide (NO) is synthesized from L-arginine by different NO synthase isozymes, which are inhibited by the substrate analogs NG-methyl- and NG-nitro-L-arginine. We studied binding of 3H-labeled NG-nitro-L-arginine to purified brain NO synthase and compared the data with results obtained in enzyme kinetic experiments. Binding data revealed a single binding site for NG-nitro-L-[3H]arginine (KD = 0.17 microM). Binding was competitively antagonized by L-arginine (KI = 2.9 microM). The half-time of dissociation was remarkably slow (9.4 min) and closely correlated with the time necessary for surmounting NO synthase inhibition by dilution. Although an apparently less potent inhibitor, NG-methyl-L-arginine exhibited the same affinity for brain NO synthase as the nitro derivative (KI = 0.17 microM), and in initial rate experiments, almost equal KI values were obtained for NG-methyl-L-arginine (0.61 microM) and NG-nitro-L-arginine (0.53 microM). However, after prolonged incubation periods, NG-nitro-L-arginine induced a rapid inactivation of the enzyme, whereas the methyl derivative turned out to be a substrate of NO synthase, which was slowly converted into stoichiometric amounts of NO and L-citrulline. | lld:pubmed |
pubmed-article:7507482 | pubmed:language | eng | lld:pubmed |
pubmed-article:7507482 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7507482 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7507482 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7507482 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7507482 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7507482 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7507482 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7507482 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7507482 | pubmed:month | Jan | lld:pubmed |
pubmed-article:7507482 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:7507482 | pubmed:author | pubmed-author:SchmidtKK | lld:pubmed |
pubmed-article:7507482 | pubmed:author | pubmed-author:MayerBB | lld:pubmed |
pubmed-article:7507482 | pubmed:author | pubmed-author:BrunnerFF | lld:pubmed |
pubmed-article:7507482 | pubmed:author | pubmed-author:KlattPP | lld:pubmed |
pubmed-article:7507482 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7507482 | pubmed:day | 21 | lld:pubmed |
pubmed-article:7507482 | pubmed:volume | 269 | lld:pubmed |
pubmed-article:7507482 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7507482 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7507482 | pubmed:pagination | 1674-80 | lld:pubmed |
pubmed-article:7507482 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:7507482 | pubmed:meshHeading | pubmed-meshheading:7507482-... | lld:pubmed |
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pubmed-article:7507482 | pubmed:meshHeading | pubmed-meshheading:7507482-... | lld:pubmed |
pubmed-article:7507482 | pubmed:year | 1994 | lld:pubmed |
pubmed-article:7507482 | pubmed:articleTitle | Inhibitors of brain nitric oxide synthase. Binding kinetics, metabolism, and enzyme inactivation. | lld:pubmed |
pubmed-article:7507482 | pubmed:affiliation | Institut für Pharmakologie und Toxikologie, Karl-Franzens-Universität Graz, Austria. | lld:pubmed |
pubmed-article:7507482 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7507482 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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